The Gordon Research Conference on Second Messengers and Protein Phosphorylation in June 1993 will concentrate on the structure and function of proteins involved in signal transduction pathways, interaction between components of these networks, and the mechanisms of modulation of their function. Considerable progress has been made in the identification of proteins involved in signal transduction. The current efforts of many laboratories is to examine the specificity of interactions among the components in the pathway. The design of the conference will bring out the multifaceted approaches currently being used to examine these questions. These approaches include genetic analysis and identification of mutations in signal transducing proteins in human disease. Also, biochemical studies to define protein-protein interactions and covalent modification of proteins will also be presented. The Conference will provide a lively forum for the exchange of information, ideas and prospects for future work. Last year approximately 80% of the participants in the conference presented data either in posters or as speakers. Such active participation by the conferees at all levels, including graduate students, postdoctoral fellows as well as junior and senior investigators, encourages discussion and fosters new interactions. The sessions planned for the 1993 Conference are: 1) Protein Kinases - Structure and Function, 2) Ligand-Regulated Ion Channels - Structure and Regulation, 3) Cyclases and Phospholipases, 4) Seven Membrane Spanning Receptors - Structure, Coupling and Signalling, 5) Heterotrimeric G Proteins - Domains, Regulation and Effector Regulation, 6) Signal Transduction Pathways Controlling Gene Expression, 7) Perturbation of Signal Transduction by Oncogenes and Viral Gene Products, 8) GTPases and Control of Cellular Functions, 9) The plenary lecture by Dr. William Catterall will provide a perspective of the structure of voltage-gated ion channels, their regulation by phosphorylation/dephosphorylation and pathologies related to toxins that influence ion channel activity.